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- PDB-6fnb: Mono- and bivalent 14-3-3 inhibitors for characterizing supramole... -

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Basic information

Entry
Database: PDB / ID: 6fnb
TitleMono- and bivalent 14-3-3 inhibitors for characterizing supramolecular lysine-PEG interactions in proteins
Components14-3-3 protein zeta/delta
KeywordsPROTEIN BINDING / Inhibition / Mono- and bivalent 14-3-3 inhibitors / Supramolecular lysine-PEG
Function / homology
Function and homology information


synaptic target recognition / Golgi reassembly / NOTCH4 Activation and Transmission of Signal to the Nucleus / establishment of Golgi localization / respiratory system process / regulation of synapse maturation / tube formation / Rap1 signalling / negative regulation of protein localization to nucleus / KSRP (KHSRP) binds and destabilizes mRNA ...synaptic target recognition / Golgi reassembly / NOTCH4 Activation and Transmission of Signal to the Nucleus / establishment of Golgi localization / respiratory system process / regulation of synapse maturation / tube formation / Rap1 signalling / negative regulation of protein localization to nucleus / KSRP (KHSRP) binds and destabilizes mRNA / GP1b-IX-V activation signalling / Regulation of localization of FOXO transcription factors / Interleukin-3, Interleukin-5 and GM-CSF signaling / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / protein targeting / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / regulation of ERK1 and ERK2 cascade / cellular response to glucose starvation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / negative regulation of TORC1 signaling / Transcriptional and post-translational regulation of MITF-M expression and activity / ERK1 and ERK2 cascade / protein sequestering activity / negative regulation of innate immune response / hippocampal mossy fiber to CA3 synapse / Translocation of SLC2A4 (GLUT4) to the plasma membrane / TP53 Regulates Metabolic Genes / Deactivation of the beta-catenin transactivating complex / lung development / Negative regulation of NOTCH4 signaling / regulation of protein stability / intracellular protein localization / melanosome / angiogenesis / DNA-binding transcription factor binding / vesicle / blood microparticle / transmembrane transporter binding / protein phosphorylation / cadherin binding / protein domain specific binding / focal adhesion / ubiquitin protein ligase binding / negative regulation of apoptotic process / protein kinase binding / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / signal transduction / extracellular space / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
14-3-3 domain / Delta-Endotoxin; domain 1 / 14-3-3 proteins signature 2. / 14-3-3 protein, conserved site / 14-3-3 proteins signature 1. / 14-3-3 protein / 14-3-3 homologues / 14-3-3 domain / 14-3-3 domain superfamily / 14-3-3 protein ...14-3-3 domain / Delta-Endotoxin; domain 1 / 14-3-3 proteins signature 2. / 14-3-3 protein, conserved site / 14-3-3 proteins signature 1. / 14-3-3 protein / 14-3-3 homologues / 14-3-3 domain / 14-3-3 domain superfamily / 14-3-3 protein / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
BENZOIC ACID / Chem-DWQ / 14-3-3 protein zeta/delta
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsBier, D. / Ottmann, C.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research FoundationCRC1093 Germany
CitationJournal: Chemistry / Year: 2018
Title: Mono- and Bivalent 14-3-3 Inhibitors for Characterizing Supramolecular "Lysine Wrapping" of Oligoethylene Glycol (OEG) Moieties in Proteins.
Authors: Yilmaz, E. / Bier, D. / Guillory, X. / Briels, J. / Ruiz-Blanco, Y.B. / Sanchez-Garcia, E. / Ottmann, C. / Kaiser, M.
History
DepositionFeb 2, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 4, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Dec 19, 2018Group: Data collection / Derived calculations / Category: struct_conn
Revision 1.3Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 14-3-3 protein zeta/delta
B: 14-3-3 protein zeta/delta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)55,95915
Polymers52,6342
Non-polymers3,32513
Water3,207178
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3630 Å2
ΔGint-82 kcal/mol
Surface area22290 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.800, 103.310, 113.060
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein 14-3-3 protein zeta/delta / Protein kinase C inhibitor protein 1 / KCIP-1


Mass: 26316.764 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: YWHAZ / Production host: Escherichia coli (E. coli) / References: UniProt: P63104

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Non-polymers , 6 types, 191 molecules

#2: Chemical ChemComp-BEZ / BENZOIC ACID


Mass: 122.121 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C7H6O2
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#5: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-DWQ / [2-[2-oxidanylidene-2-[[3-[2-[5-[3-oxidanylidene-3-[3-[2-[2-[3-[3-[2-[2-[2-[[3-[2-(2-phosphonophenoxy)ethanoylamino]phenyl]carbonylamino]ethoxy]ethoxy]ethoxy]propanoylamino]propoxy]ethoxy]ethoxy]propylamino]propoxy]pentoxy]ethylcarbamoyl]phenyl]amino]ethoxy]phenyl]phosphonic acid


Mass: 1291.273 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C59H84N6O22P2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 178 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.98 Å3/Da / Density % sol: 69.12 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, sitting drop
Details: 0.09 M HEPES sodium salt pH 7.5 1.26 M tri-Sodium citrate 10 %(v/v) Glycerol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 20, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3→46.98 Å / Num. obs: 38130 / % possible obs: 100 % / Redundancy: 13.252 % / Biso Wilson estimate: 60.572 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.128 / Rrim(I) all: 0.134 / Χ2: 0.95 / Net I/σ(I): 12.09 / Num. measured all: 505296 / Scaling rejects: 27
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.3-2.413.041.1062.4258603449744940.8581.15199.9
2.4-2.513.950.8413.2753037380238020.9260.872100
2.5-313.360.3546.7216546912385123850.9830.368100
3-413.3280.12617.45132023990699060.9940.131100
4-612.9630.09723.8467747522652260.9960.101100
6-812.9310.10224.716836130313020.9960.10699.9
8-1011.6670.09724.7855074724720.9940.101100
10-1210.7910.09523.8723742212200.9940.10199.5
12-1412.0350.09325.3513841151150.9950.098100
14-2011.880.08925.2715801331330.9980.092100
20-409.8170.09321.9569771710.9970.098100
40-46.989.750.08224391440.9960.08628.6

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation2.5 Å46.98 Å
Translation2.5 Å46.98 Å

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Processing

Software
NameVersionClassificationNB
REFMACrefinement
XDSdata reduction
XSCALEdata scaling
PHASER2.3.0phasing
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NKX

3nkx


Resolution: 2.3→46.98 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.946 / SU B: 7.254 / SU ML: 0.163 / SU R Cruickshank DPI: 0.2152 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.215 / ESU R Free: 0.189
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2484 1904 5 %RANDOM
Rwork0.2143 ---
obs0.216 36165 99.97 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 137.39 Å2 / Biso mean: 60.153 Å2 / Biso min: 36.23 Å2
Baniso -1Baniso -2Baniso -3
1--1.91 Å2-0 Å20 Å2
2--5.66 Å20 Å2
3----3.76 Å2
Refinement stepCycle: final / Resolution: 2.3→46.98 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3532 0 122 179 3833
Biso mean--60.76 63.97 -
Num. residues----457
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.023698
X-RAY DIFFRACTIONr_bond_other_d0.0020.023361
X-RAY DIFFRACTIONr_angle_refined_deg1.0721.9964981
X-RAY DIFFRACTIONr_angle_other_deg0.8793.0077769
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.9455453
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.6225.03165
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.10815632
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.3521521
X-RAY DIFFRACTIONr_chiral_restr0.0550.2558
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.024096
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02737
LS refinement shellResolution: 2.3→2.36 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.331 139 -
Rwork0.321 2630 -
all-2769 -
obs--99.93 %

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